Sequence and intramolecular distance scoring analyses of microbial rhodopsins [version 2; referees: 2 approved]
Recent accumulation of sequence and structural data, in conjunction with systematical classification into a set of families, has significantly advanced our understanding of diverse and specific protein functions. Analysis and interpretation of protein family data requires comprehensive sequence and...
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doaj-cf737700a1414d2a9985ee7f945a90792020-11-25T03:06:38ZengF1000 Research LtdF1000Research2046-14022016-04-01510.12688/f1000research.7920.29078Sequence and intramolecular distance scoring analyses of microbial rhodopsins [version 2; referees: 2 approved]Miki Asano0Shunta Ide1Atsushi Kamata2Kiyohiro Takahasi3Tetsuji Okada4Department of Life Science, Gakushuin University, Tokyo, JapanDepartment of Life Science, Gakushuin University, Tokyo, JapanDepartment of Life Science, Gakushuin University, Tokyo, JapanDepartment of Life Science, Gakushuin University, Tokyo, JapanDepartment of Life Science, Gakushuin University, Tokyo, JapanRecent accumulation of sequence and structural data, in conjunction with systematical classification into a set of families, has significantly advanced our understanding of diverse and specific protein functions. Analysis and interpretation of protein family data requires comprehensive sequence and structural alignments. Here, we present a simple scheme for analyzing a set of experimental structures of a given protein or family of proteins, using microbial rhodopsins as an example. For a data set comprised of around a dozen highly similar structures to each other (overall pairwise root-mean-squared deviation < 2.3 Å), intramolecular distance scoring analysis yielded valuable information with respect to structural properties, such as differences in the relative variability of transmembrane helices. Furthermore, a comparison with recent results for G protein-coupled receptors demonstrates how the results of the present analysis can be interpreted and effectively utilized for structural characterization of diverse protein families in general.http://f1000research.com/articles/5-165/v2BioinformaticsProtein Chemistry & Proteomics |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Miki Asano Shunta Ide Atsushi Kamata Kiyohiro Takahasi Tetsuji Okada |
spellingShingle |
Miki Asano Shunta Ide Atsushi Kamata Kiyohiro Takahasi Tetsuji Okada Sequence and intramolecular distance scoring analyses of microbial rhodopsins [version 2; referees: 2 approved] F1000Research Bioinformatics Protein Chemistry & Proteomics |
author_facet |
Miki Asano Shunta Ide Atsushi Kamata Kiyohiro Takahasi Tetsuji Okada |
author_sort |
Miki Asano |
title |
Sequence and intramolecular distance scoring analyses of microbial rhodopsins [version 2; referees: 2 approved] |
title_short |
Sequence and intramolecular distance scoring analyses of microbial rhodopsins [version 2; referees: 2 approved] |
title_full |
Sequence and intramolecular distance scoring analyses of microbial rhodopsins [version 2; referees: 2 approved] |
title_fullStr |
Sequence and intramolecular distance scoring analyses of microbial rhodopsins [version 2; referees: 2 approved] |
title_full_unstemmed |
Sequence and intramolecular distance scoring analyses of microbial rhodopsins [version 2; referees: 2 approved] |
title_sort |
sequence and intramolecular distance scoring analyses of microbial rhodopsins [version 2; referees: 2 approved] |
publisher |
F1000 Research Ltd |
series |
F1000Research |
issn |
2046-1402 |
publishDate |
2016-04-01 |
description |
Recent accumulation of sequence and structural data, in conjunction with systematical classification into a set of families, has significantly advanced our understanding of diverse and specific protein functions. Analysis and interpretation of protein family data requires comprehensive sequence and structural alignments. Here, we present a simple scheme for analyzing a set of experimental structures of a given protein or family of proteins, using microbial rhodopsins as an example. For a data set comprised of around a dozen highly similar structures to each other (overall pairwise root-mean-squared deviation < 2.3 Å), intramolecular distance scoring analysis yielded valuable information with respect to structural properties, such as differences in the relative variability of transmembrane helices. Furthermore, a comparison with recent results for G protein-coupled receptors demonstrates how the results of the present analysis can be interpreted and effectively utilized for structural characterization of diverse protein families in general. |
topic |
Bioinformatics Protein Chemistry & Proteomics |
url |
http://f1000research.com/articles/5-165/v2 |
work_keys_str_mv |
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